The glycosylation pattern of baculovirus expressed envelope protein E2 affects its ability to prevent infection with bovine viral diarrhoea virus

We have investigated the role of glycosylation of the envelope glycoprotein E2 of bovine viral diarrhoea virus (BVDV), produced in insect cells, in BVDV infection. When amino acids predicated to code for the C-terminal N-linked glycosylation site were mutated the resulting protein was less efficient...

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Bibliographic Details
Published in:Virus research 2005-12, Vol.114 (1), p.54-62
Main Authors: Pande, A., Carr, B.V., Wong, S.Y.C., Dalton, K., Jones, I.M., McCauley, J.W., Charleston, B.
Format: Article
Language:English
Subjects:
Animals
Baculoviridae - genetics
Baculoviridae - metabolism
Baculovirus
Bovine viral diarrhea virus
Cattle
Cells, Cultured
Diarrhea Viruses, Bovine Viral - genetics
Diarrhea Viruses, Bovine Viral - metabolism
Diarrhea Viruses, Bovine Viral - pathogenicity
Glycosylation
Male
Mutagenesis, Site-Directed
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Spodoptera - virology
Testis - cytology
Testis - virology
Viral Envelope Proteins - genetics
Viral Envelope Proteins - metabolism
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Summary:We have investigated the role of glycosylation of the envelope glycoprotein E2 of bovine viral diarrhoea virus (BVDV), produced in insect cells, in BVDV infection. When amino acids predicated to code for the C-terminal N-linked glycosylation site were mutated the resulting protein was less efficient than wild type protein at preventing infection of susceptible cells with BVDV. In addition, mutational analysis showed that a further two predicted N-terminal N-linked glycosylation sites of E2 are required for efficient production of recombinant protein.
ISSN:0168-1702
1872-7492
DOI:10.1016/j.virusres.2005.05.011